Isolation of two types of Pseudomonas aeruginosa mutants highly sensitive to a specific group of beta-lactam antibiotics and with defect in penicillin-binding proteins.
Two types of mutants highly sensitive to beta-lactam antibiotics were obtained from Pseudomonas aeruginosa PAO 2142 by treatment with N-methyl-N'-nitro-N-nitrosoguanidine. One type of mutant showed over 30 times higher sensitivity to mecillinam, carbenicillin and sulbenicillin than did the parent, but not to most other beta-lactam antibiotics tested. In contrast, the other type mutant was about 30 times more sensitive to ampicillin, cephaloridine, cefoxitin and cefmetazole, but resistant to mecillinam, carbenicillin and sulbenicillin at the same level as the parent. Beta-lactamase activity of these mutants ws not different from that of the parent. Defect in either of penicillin-binding proteins 1A/1B or 5 was observed in some mutants of P. aeruginosa highly sensitive to beta-lactam antibiotics.
D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000172:deficiency*; D004352:Drug Resistance, Microbial; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; D009154:Mutation; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D011550:Pseudomonas aeruginosa / Q000187:drug effects / Q000201:enzymology / Q000302:isolation & purification*; D001618:beta-Lactamases / Q000378:metabolism; D047090:beta-Lactams / Q000494:pharmacology
D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D047090:beta-Lactams; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; D001618:beta-Lactamases